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Protein

2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase

Gene

mhpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively.1 Publication

Catalytic activityi

3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate.
(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate.

Kineticsi

  1. KM=26 µM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8)2 Publications
  2. KM=36 µM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8)2 Publications
  3. KM=37 µM for methyl-2,3-dihydroxyphenylpropionate (at 20 degrees Celsius and pH 8)2 Publications
  4. KM=90 µM for 3-methylcatechol (at 20 degrees Celsius and pH 8)2 Publications
  5. KM=94 µM for 3-phenethylcatechol (at 20 degrees Celsius and pH 8)2 Publications
  6. KM=154 µM for 3-propylcatechol (at 20 degrees Celsius and pH 8)2 Publications
  7. KM=185 µM for 3-ethylcatechol (at 20 degrees Celsius and pH 8)2 Publications
  8. KM=300 µM for 2,3-dihydroxyphenoxyacetic acid (at 20 degrees Celsius and pH 8)2 Publications
  9. KM=700 µM for catechol (at 20 degrees Celsius and pH 8)2 Publications

    Pathwayi: 3-phenylpropanoate degradation

    This protein is involved in the pathway 3-phenylpropanoate degradation, which is part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the pathway 3-phenylpropanoate degradation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei115Proton donor1
    Active sitei179Proton acceptor1

    GO - Molecular functioni

    • 3-carboxyethylcatechol 2,3-dioxygenase activity Source: EcoCyc
    • ferrous iron binding Source: EcoCyc

    GO - Biological processi

    • 3-(3-hydroxy)phenylpropionate catabolic process Source: EcoCyc
    • 3-phenylpropionate catabolic process Source: UniProtKB-UniPathway
    • phenylpropanoid catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    Iron

    Enzyme and pathway databases

    BioCyciEcoCyc:DHPDIOXYGEN-MONOMER.
    ECOL316407:JW0339-MONOMER.
    MetaCyc:DHPDIOXYGEN-MONOMER.
    BRENDAi1.13.11.16. 2026.
    SABIO-RKP0ABR9.
    UniPathwayiUPA00714.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase (EC:1.13.11.16)
    Alternative name(s):
    3-carboxyethylcatechol 2,3-dioxygenase
    Gene namesi
    Name:mhpB
    Ordered Locus Names:b0348, JW0339
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG20274. mhpB.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi114D → A: Complete loss of extradiol cleavage activity. 1 Publication1
    Mutagenesisi114D → N: Low level of catalytic activity, 600-fold lower than the wild-type enzyme. More than 8000-fold decrease in affinity. 1 Publication1
    Mutagenesisi115H → A: Complete loss of extradiol cleavage activity. 1 Publication1
    Mutagenesisi115H → Q: Complete loss of activity. 1 Publication1
    Mutagenesisi115H → Y: Complete loss of activity. 1 Publication1
    Mutagenesisi179H → A: Complete loss of activity. 1 Publication1
    Mutagenesisi179H → Q: Complete loss of activity. 1 Publication1
    Mutagenesisi179H → Y: Complete loss of activity. 1 Publication1
    Mutagenesisi181P → A: More than 2-fold decrease in catalytic activity and 100-fold decrease in affinity. 1 Publication1
    Mutagenesisi181P → H: More than 60-fold decrease in catalytic activity and affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000851031 – 3142,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenaseAdd BLAST314

    Proteomic databases

    PaxDbiP0ABR9.
    PRIDEiP0ABR9.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi4260730. 12 interactors.
    DIPiDIP-10206N.
    IntActiP0ABR9. 12 interactors.
    STRINGi511145.b0348.

    Structurei

    3D structure databases

    ProteinModelPortaliP0ABR9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105MI0. Bacteria.
    ENOG410XPPS. LUCA.
    HOGENOMiHOG000069851.
    InParanoidiP0ABR9.
    KOiK05713.
    OMAiHCLSHTP.

    Family and domain databases

    CDDicd07365. MhpB_like. 1 hit.
    Gene3Di3.40.830.10. 2 hits.
    HAMAPiMF_01653. MhpB. 1 hit.
    InterProiIPR023789. DHPP/DHXA_dioxygenase.
    IPR004183. Xdiol_dOase_suB.
    [Graphical view]
    PfamiPF02900. LigB. 1 hit.
    [Graphical view]
    SUPFAMiSSF53213. SSF53213. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P0ABR9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA
    60 70 80 90 100
    PDHYNGFFYD VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK
    110 120 130 140 150
    SGIDLAVSYC MQVDHGFAQP LEFLLGGLDK VPVLPVFING VATPLPGFQR
    160 170 180 190 200
    TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ PPVPELAKAD AHMRDRLLGS
    210 220 230 240 250
    GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ FMTLLEQGRI
    260 270 280 290 300
    QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISAFGNWRS EGRYYRPIPE
    310
    WIAGFGSLSA RTEN
    Length:314
    Mass (Da):34,196
    Last modified:November 8, 2005 - v1
    Checksum:iE1D5A8574E5DFE05
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti138 – 140ING → NKA in BAA13053 (PubMed:8752345).Curated3
    Sequence conflicti152R → H in BAA13053 (PubMed:8752345).Curated1
    Sequence conflicti157A → T in BAA13053 (PubMed:8752345).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D86239 Genomic DNA. Translation: BAA13053.1.
    Y09555 Genomic DNA. Translation: CAA70748.1.
    U73857 Genomic DNA. Translation: AAB18072.1.
    U00096 Genomic DNA. Translation: AAC73451.1.
    AP009048 Genomic DNA. Translation: BAE76130.1.
    PIRiD64762.
    RefSeqiNP_414882.1. NC_000913.3.
    WP_000543457.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73451; AAC73451; b0348.
    BAE76130; BAE76130; BAE76130.
    GeneIDi945047.
    KEGGiecj:JW0339.
    eco:b0348.
    PATRICi32115829. VBIEscCol129921_0356.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D86239 Genomic DNA. Translation: BAA13053.1.
    Y09555 Genomic DNA. Translation: CAA70748.1.
    U73857 Genomic DNA. Translation: AAB18072.1.
    U00096 Genomic DNA. Translation: AAC73451.1.
    AP009048 Genomic DNA. Translation: BAE76130.1.
    PIRiD64762.
    RefSeqiNP_414882.1. NC_000913.3.
    WP_000543457.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP0ABR9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260730. 12 interactors.
    DIPiDIP-10206N.
    IntActiP0ABR9. 12 interactors.
    STRINGi511145.b0348.

    Proteomic databases

    PaxDbiP0ABR9.
    PRIDEiP0ABR9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73451; AAC73451; b0348.
    BAE76130; BAE76130; BAE76130.
    GeneIDi945047.
    KEGGiecj:JW0339.
    eco:b0348.
    PATRICi32115829. VBIEscCol129921_0356.

    Organism-specific databases

    EchoBASEiEB4167.
    EcoGeneiEG20274. mhpB.

    Phylogenomic databases

    eggNOGiENOG4105MI0. Bacteria.
    ENOG410XPPS. LUCA.
    HOGENOMiHOG000069851.
    InParanoidiP0ABR9.
    KOiK05713.
    OMAiHCLSHTP.

    Enzyme and pathway databases

    UniPathwayiUPA00714.
    BioCyciEcoCyc:DHPDIOXYGEN-MONOMER.
    ECOL316407:JW0339-MONOMER.
    MetaCyc:DHPDIOXYGEN-MONOMER.
    BRENDAi1.13.11.16. 2026.
    SABIO-RKP0ABR9.

    Miscellaneous databases

    PROiP0ABR9.

    Family and domain databases

    CDDicd07365. MhpB_like. 1 hit.
    Gene3Di3.40.830.10. 2 hits.
    HAMAPiMF_01653. MhpB. 1 hit.
    InterProiIPR023789. DHPP/DHXA_dioxygenase.
    IPR004183. Xdiol_dOase_suB.
    [Graphical view]
    PfamiPF02900. LigB. 1 hit.
    [Graphical view]
    SUPFAMiSSF53213. SSF53213. 2 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMHPB_ECOLI
    AccessioniPrimary (citable) accession number: P0ABR9
    Secondary accession number(s): P54711
    , P77048, P77461, Q2MC76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: November 2, 2016
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.